Albumin, Acetylated from bovine serum

Acetylated bovine serum albumin has been used:

• as a component of protease buffer for protease inhibition assay
• as a blocking agent in the preparation of cDNA glass array
• to select hybridoma antibodies sensitive to M-ficolin epitopes by immunofluorometric assay

Acetylated to inactivate nucleases commonly found in BSA. Acetylated BSA should not be used as a protein standard since acetylation of tyrosine residues prevents color development in the Lowry assay and other similar protein determinations.

This B2518 acetylated BSA product has been cited in various publications and protocols, such as the following:






* As an electrophoresis standard: Lindberg, T. et al., J. Pediatr. Gastroenterol. Nutr., 27(1), 30-36 (1998)




* In in situ end-labeling buffer for labeling of DNA fragments: Save, V. et al., ”Detecting and Quantifying Apoptosis in Tissue Sections”, in Apoptosis Methods and Protocols (H.J.M. Brady, ed.). Methods Mol. Biol., Vol. 282, pp. 67-84 (2004)




* In EMSA studies on nucleocytoplasmic shuttling: Ghosh, C.C. et al., “Analysis of Nucleocytoplasmic Shuttling of NF?B Proteins in Human Leukocytes”, in Membrane Trafficking (A. Vancura, ed.). Methods Mol. Biol., Vol. 457, pp. 279-292 (2008)




* In selection buffer for ribosome display studies: Larman, H.B. et al., Nat. Protoc., 9(1), 90-103 (2014)

Native bovine serum albumin (BSA) acts as a transporter of drugs, hormones and fatty acids. It has calcium binding sites and regulates metal homeostasis.

Native bovine serum albumin (BSA) is a 66 kDa protein, which belongs to the family of serum albumin. It consists of three domains (I, II and III) and is the major protein found in circulatory system. Native BSA is an α-helical, globular and non-glycosylated protein, with 17-disulfide bonds.

Acetylation of bovine serum albumin modifies various residues, most notably lysine (Lys), and also serine (Ser) and threonine (Thr) to lesser extents. MALDI-TOF mass spectrometry studies on acetylated BSA have indicated a MW value about 3000 Da higher compared to native BSA (Ostatná, V. et al., J. Electroanalytical Chem., 821, 97-103 (2018)).. Acetylation of BSA also modifies parallel amino acid residues in any trace contaminating nucleases in the BSA, which inactivates that trace nuclease content. Thus acetylated BSA can be used in molecular biology applications where trace nuclease activity must be minimized.